COLI_SHEEP
ID COLI_SHEEP Reviewed; 263 AA.
AC P01191; Q28826; Q8MIC5;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 11-DEC-2013, sequence version 3.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Pro-opiomelanocortin;
DE Short=POMC;
DE AltName: Full=Corticotropin-lipotropin;
DE Contains:
DE RecName: Full=NPP;
DE Contains:
DE RecName: Full=Melanotropin gamma;
DE AltName: Full=Gamma-MSH;
DE Contains:
DE RecName: Full=Corticotropin;
DE AltName: Full=Adrenocorticotropic hormone;
DE Short=ACTH;
DE Contains:
DE RecName: Full=Melanocyte-stimulating hormone alpha;
DE Short=Alpha-MSH;
DE AltName: Full=Melanotropin alpha;
DE Contains:
DE RecName: Full=Corticotropin-like intermediary peptide;
DE Short=CLIP;
DE Contains:
DE RecName: Full=Lipotropin beta;
DE AltName: Full=Beta-LPH;
DE Contains:
DE RecName: Full=Lipotropin gamma;
DE AltName: Full=Gamma-LPH;
DE Contains:
DE RecName: Full=Melanocyte-stimulating hormone beta;
DE Short=Beta-MSH;
DE AltName: Full=Melanotropin beta;
DE Contains:
DE RecName: Full=Beta-endorphin;
DE Contains:
DE RecName: Full=Met-enkephalin;
DE Flags: Precursor;
GN Name=POMC;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC STRAIN=Ile de France; TISSUE=Hypothalamus;
RX PubMed=14636633; DOI=10.1016/s0016-6480(03)00266-1;
RA Pillon D., Caraty A., Fabre-Nys C., Bruneau G.;
RT "Early decrease of proopiomelanocortin but not neuropeptide Y mRNA
RT expression in the mediobasal hypothalamus of the ewe, during the estradiol-
RT induced preovulatory LH surge.";
RL Gen. Comp. Endocrinol. 134:264-272(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 52-136.
RX PubMed=8384993; DOI=10.1210/endo.132.4.8384993;
RA Levin N., Wallace C., Bengani N., Blum M., Farnworth P., Smith A.I.,
RA Roberts J.L.;
RT "Ovine anterior pituitary proopiomelanocortin gene expression is not
RT increased by ACTH secretagogues in vitro.";
RL Endocrinology 132:1692-1700(1993).
RN [3]
RP PROTEIN SEQUENCE OF 132-170.
RA Leonis J., Li C.H., Chung D.;
RT "Corticotropins (ACTH). XV. The action of chymotrypsin on alpha-
RT corticotropin.";
RL J. Am. Chem. Soc. 81:419-423(1959).
RN [4]
RP PROTEIN SEQUENCE OF 132-170, AND SEQUENCE REVISION.
RX PubMed=4344689; DOI=10.1016/0006-291x(72)90486-x;
RA Li C.H.;
RT "Adrenocorticotropin 45. Revised amino acid sequences for sheep and bovine
RT hormones.";
RL Biochem. Biophys. Res. Commun. 49:835-839(1972).
RN [5]
RP PROTEIN SEQUENCE OF 132-170, AND SEQUENCE REVISION.
RX PubMed=4370084; DOI=10.1016/0014-5793(74)80838-0;
RA Joehl A., Riniker B., Schenkel-Hulliger L.;
RT "Identity of structure of ovine and bovine ACTH: correction of revised
RT structure of the ovine hormone.";
RL FEBS Lett. 45:172-174(1974).
RN [6]
RP PROTEIN SEQUENCE OF 132-144 AND 213-230, ACETYLATION AT SER-132, AND
RP AMIDATION AT VAL-144.
RX PubMed=13929167; DOI=10.1016/0006-3002(63)91144-2;
RA Lee T.H., Lerner A.B., Buettner-Janusch V.;
RT "Melanocyte-stimulating hormones from sheep pituitary glands.";
RL Biochim. Biophys. Acta 71:706-709(1963).
RN [7]
RP PROTEIN SEQUENCE OF 173-263.
RX PubMed=4162144; DOI=10.1038/2081093b0;
RA Li C.H., Barnafi L., Chretien M., Chung D.;
RT "Isolation and amino-acid sequence of beta-LPH from sheep pituitary
RT glands.";
RL Nature 208:1093-1094(1965).
RN [8]
RP PROTEIN SEQUENCE OF 173-263, AND SEQUENCE REVISION.
RX PubMed=4675453; DOI=10.1111/j.1399-3011.1972.tb03427.x;
RA Chretien M., Gilardeau C., Li C.H.;
RT "Revised structure of sheep beta-lipotropic hormone.";
RL Int. J. Pept. Protein Res. 4:263-265(1972).
RN [9]
RP PROTEIN SEQUENCE OF 173-263, AND SEQUENCE REVISION.
RX PubMed=4270658; DOI=10.1016/0006-291x(73)90607-4;
RA Graf L., Li C.H.;
RT "Action of plasmin on ovine beta-lipotropin: revision of the carboxyl
RT terminal sequence.";
RL Biochem. Biophys. Res. Commun. 53:1304-1309(1973).
RN [10]
RP PROTEIN SEQUENCE OF 233-263.
RX PubMed=843377; DOI=10.1016/0006-291x(77)90616-7;
RA Seidah N.G., Dragon N., Benjannet S., Routhier R., Chretien M.;
RT "The complete sequence of sheep beta-endorphin.";
RL Biochem. Biophys. Res. Commun. 74:1528-1535(1977).
CC -!- FUNCTION: [Corticotropin]: Stimulates the adrenal glands to release
CC cortisol.
CC -!- FUNCTION: [Melanocyte-stimulating hormone alpha]: Anorexigenic peptide.
CC Increases the pigmentation of skin by increasing melanin production in
CC melanocytes.
CC -!- FUNCTION: [Melanocyte-stimulating hormone beta]: Increases the
CC pigmentation of skin by increasing melanin production in melanocytes.
CC -!- FUNCTION: [Beta-endorphin]: Endogenous orexigenic opiate.
CC -!- FUNCTION: [Met-enkephalin]: Endogenous opiate.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01193}.
CC Note=Melanocyte-stimulating hormone alpha and beta-endorphin are stored
CC in separate granules in hypothalamic POMC neurons, suggesting that
CC secretion may be under the control of different regulatory mechanisms.
CC {ECO:0000250|UniProtKB:P01193}.
CC -!- TISSUE SPECIFICITY: ACTH and MSH are produced by the pituitary gland.
CC -!- INDUCTION: Repressed by treatment with estradiol.
CC {ECO:0000269|PubMed:14636633}.
CC -!- PTM: Specific enzymatic cleavages at paired basic residues yield the
CC different active peptides.
CC -!- SIMILARITY: Belongs to the POMC family. {ECO:0000305}.
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DR EMBL; AJ507201; CAD45184.1; -; mRNA.
DR EMBL; S57982; AAB26022.1; -; mRNA.
DR PIR; A49188; CTSHP.
DR RefSeq; NP_001009266.1; NM_001009266.1.
DR AlphaFoldDB; P01191; -.
DR BMRB; P01191; -.
DR SMR; P01191; -.
DR STRING; 9940.ENSOARP00000019583; -.
DR iPTMnet; P01191; -.
DR GeneID; 443212; -.
DR KEGG; oas:443212; -.
DR CTD; 5443; -.
DR eggNOG; ENOG502RZNY; Eukaryota.
DR OrthoDB; 1168862at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR013531; Mcrtin_ACTH_cent.
DR InterPro; IPR013593; Melanocortin_N.
DR InterPro; IPR013532; Opioid_neuropept.
DR InterPro; IPR001941; PMOC.
DR Pfam; PF00976; ACTH_domain; 3.
DR Pfam; PF08384; NPP; 1.
DR Pfam; PF08035; Op_neuropeptide; 1.
DR PRINTS; PR00383; MELANOCORTIN.
DR SMART; SM01363; ACTH_domain; 3.
DR SMART; SM01364; NPP; 1.
DR SMART; SM01365; Op_neuropeptide; 1.
PE 1: Evidence at protein level;
KW Acetylation; Amidation; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Endorphin; Glycoprotein;
KW Hormone; Phosphoprotein; Pyrrolidone carboxylic acid; Reference proteome;
KW Secreted; Signal; Sulfation.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PEPTIDE 27..103
FT /note="NPP"
FT /id="PRO_0000025039"
FT PEPTIDE 77..87
FT /note="Melanotropin gamma"
FT /id="PRO_0000025040"
FT PROPEP 106..129
FT /id="PRO_0000424695"
FT PEPTIDE 132..170
FT /note="Corticotropin"
FT /id="PRO_0000025041"
FT PEPTIDE 132..144
FT /note="Melanocyte-stimulating hormone alpha"
FT /id="PRO_0000025042"
FT PEPTIDE 150..170
FT /note="Corticotropin-like intermediary peptide"
FT /id="PRO_0000025043"
FT PEPTIDE 173..263
FT /note="Lipotropin beta"
FT /id="PRO_0000025044"
FT PEPTIDE 173..230
FT /note="Lipotropin gamma"
FT /id="PRO_0000025045"
FT PEPTIDE 213..230
FT /note="Melanocyte-stimulating hormone beta"
FT /id="PRO_0000025046"
FT PEPTIDE 233..263
FT /note="Beta-endorphin"
FT /id="PRO_0000025047"
FT PEPTIDE 233..237
FT /note="Met-enkephalin"
FT /id="PRO_0000025048"
FT REGION 94..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 87
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250|UniProtKB:P01190"
FT MOD_RES 132
FT /note="N-acetylserine; in Corticotropin"
FT /evidence="ECO:0000269|PubMed:13929167"
FT MOD_RES 144
FT /note="Valine amide"
FT /evidence="ECO:0000269|PubMed:13929167"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01189"
FT MOD_RES 173
FT /note="Pyrrolidone carboxylic acid (Glu); partial"
FT /evidence="ECO:0000250"
FT MOD_RES 200
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT CARBOHYD 71
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..50
FT /evidence="ECO:0000250"
FT DISULFID 34..46
FT /evidence="ECO:0000250"
FT CONFLICT 65
FT /note="G -> C (in Ref. 2; AAB26022)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 263 AA; 29062 MW; ECB3A6E9AFB9DE81 CRC64;
MPRLCSSRSG ALLLVLLLQA SMEVRGWCLE SSQCQDLTTE SNLLACIRAC KPDLSAETPV
FPGNGDEQPL TENPRKYVMG HFRWDRFGRR NGSSSFGAGG AAQKREEEVA VGEGPGPRGD
GAETGPREDK RSYSMEHFRW GKPVGKKRRP VKVYPNGAED ESAQAFPLEF KRELTGERLE
QARGPEAQAE SAAARAELEY GLVAEAEAAE KKDSGPYKME HFRWGSPPKD KRYGGFMTSE
KSQTPLVTLF KNAIIKNAHK KGQ
